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Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway

Academic Article
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Overview

authors

  • Cantin, G. T.
  • Venable, J. D.
  • Cociorva, D.
  • Yates III, John

publication date

  • January 2006

journal

  • Journal of Proteome Research  Journal

abstract

  • Protein phosphorylation has become a focus of many proteomic studies due to the central role that it plays in biology. We combine peptide-based gel-free isoelectric focusing and immobilized metal affinity chromatography to enhance the detection of phosphorylation events within complex protein samples using LC-MS. This method is then used to carry out a quantitative phosphoproteomic analysis of the tumor necrosis factor (TNF) pathway using HeLa cells metabolically labeled with 15N-containing amino acids, where 145 phosphorylation sites were found to be up-regulated upon the activation of the TNF pathway.

subject areas

  • Chromatography, Affinity
  • Chromatography, Liquid
  • HeLa Cells
  • Humans
  • Isoelectric Focusing
  • Isotope Labeling
  • Mass Spectrometry
  • Nitrogen Isotopes
  • Peptide Fragments
  • Phosphopeptides
  • Phosphoproteins
  • Phosphorylation
  • Proteome
  • Proteomics
  • Tumor Necrosis Factor-alpha
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Research

keywords

  • IMAC
  • PKA
  • TNF
  • apoptosis
  • isoelectric focusing
  • metabolic labeling
  • phosphoproteome
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Identity

PubMed Central ID

  • PMC2570265

International Standard Serial Number (ISSN)

  • 1535-3893

Digital Object Identifier (DOI)

  • 10.1021/pr050270m

PubMed ID

  • 16396503
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Additional Document Info

start page

  • 127

end page

  • 134

volume

  • 5

issue

  • 1

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